NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2522989786|gb|WJH92612|]
View 

2Fe-2S iron-sulfur cluster binding domain-containing protein [Mycobacterium tuberculosis complex sp. N0157]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 104-333 7.25e-111

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


:

Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 338.03  E-value: 7.25e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 104 TGDGVVTAVELVSPSTAILRVDTSGMaGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRgECEFIIRLLPDGVMSNYLR 183
Cdd:cd06209     1 TFEATVTEVERLSDSTIGLTLELDEA-GALAFLPGQYVNLQVPGTDETRSYSFSSAPGDP-RLEFLIRLLPGGAMSSYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADV-AHPVYLLYGVERTEDLCKLDELTELRRRV 262
Cdd:cd06209    79 DRAQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGsAHPVHLVYGVTRDADLVELDRLEALAERL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 263 GRLEVHVVVARPDPdWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06209   159 PGFSFRTVVADPDS-WHPRKGYVTDHLEAEDLNDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-91 3.56e-23

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.14  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   1 MAvrQVTVgysDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQ 80
Cdd:COG0633     1 MP--KVTF---IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQ 75

                          90
                  ....*....|.
gi 2522989786  81 TFVTSDCRIEL 91
Cdd:COG0633    76 ARPTSDLVVEL 86
UbiH super family cl43226
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 364-551 1.16e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


The actual alignment was detected with superfamily member COG0654:

Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 41.85  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 364 AVVIGGSIAGIAAAKMLSETFDRVIVLEKDgPHRRREGRPGAaqgwhLHHlltAGQIELERIfpGIVDDMVREGAfkVDM 443
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERA-PPPRPDGRGIA-----LSP---RSLELLRRL--GLWDRLLARGA--PIR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 444 AAQYRIRLGGTWKK----PGTSDIEIVCAGRPLLEWCVRRRLDDEPrIDFRYESEVADLAFDRAnnaivGVAVDNGDAdg 519
Cdd:COG0654    73 GIRVRDGSDGRVLArfdaAETGLPAGLVVPRADLERALLEAARALG-VELRFGTEVTGLEQDAD-----GVTVTLADG-- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2522989786 520 gdglQVVPAEFVVDASGKNTRVPEFLERLGVG 551
Cdd:COG0654   145 ----RTLRADLVVGADGARSAVRRLLGIGFTG 172
 
Name Accession Description Interval E-value
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 104-333 7.25e-111

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 338.03  E-value: 7.25e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 104 TGDGVVTAVELVSPSTAILRVDTSGMaGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRgECEFIIRLLPDGVMSNYLR 183
Cdd:cd06209     1 TFEATVTEVERLSDSTIGLTLELDEA-GALAFLPGQYVNLQVPGTDETRSYSFSSAPGDP-RLEFLIRLLPGGAMSSYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADV-AHPVYLLYGVERTEDLCKLDELTELRRRV 262
Cdd:cd06209    79 DRAQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGsAHPVHLVYGVTRDADLVELDRLEALAERL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 263 GRLEVHVVVARPDPdWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06209   159 PGFSFRTVVADPDS-WHPRKGYVTDHLEAEDLNDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
5-337 2.75e-104

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 325.55  E-value: 2.75e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   5 QVTVGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRT--EGLSDVERAARKILTCQTF 82
Cdd:PRK11872    4 KVALSFADGKTLFFPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDYVdeDALSERDLAQRKMLACQTR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  83 VTSDCRIELQYPVD-DNAALLVTGDGVVTAVELVSPSTAILRVDTSGMAGALRYRAGQFAQLQVPGTNVWRNYSYAHPAD 161
Cdd:PRK11872   84 VKSDAAFYFDFDSSlCNAGDTLKISGVVTAVELVSETTAILHLDASAHGRQLDFLPGQYARLQIPGTDDWRSYSFANRPN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 162 GRGECEFIIRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSL-DADVAHPVYLL 240
Cdd:PRK11872  164 ATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAFYLREVERPLVFVAGGTGLSAFLGMLDELaEQGCSPPVHLY 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 241 YGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHN 320
Cdd:PRK11872  244 YGVRHAADLCELQRLAAYAERLPNFRYHPVVSKASADWQGKRGYIHEHFDKAQLRDQAFDMYLCGPPPMVEAVKQWLDEQ 323

                         330
                  ....*....|....*..
gi 2522989786 321 GFHRVGLYYEKFVASGA 337
Cdd:PRK11872  324 ALENYRLYYEKFTQSNT 340
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
23-335 6.18e-92

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 292.50  E-value: 6.18e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  23 DQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRT---EGLSDVERAARKILTCQTFVTSDCRIELQYPvddnA 99
Cdd:NF040810   20 GETVLDAAYRQKINIPMDCRDGACGTCKCRCESGSYDLGDDyieDALTEEEAAQGYVLTCQMVPQSDCVIRVPAS----S 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 100 ALLVTG----DGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQVPGTNVWRNYSYAHPAdGRGECEFIIRLLPD 175
Cdd:NF040810   96 AACKTGqatfEATVAAVEQLSDSTIELSLDLDD-DAALAFLPGQYVNIQVPGTGQTRSYSFSSLP-GAREASFLIRNVPG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 176 GVMSNYLRDRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDAD-VAHPVYLLYGVERTEDLCKLDE 254
Cdd:NF040810  174 GLMSSYLTERAKPGDRLSLTGPLGSFYLREVTRPLLMLAGGTGLAPFLSMLEVLAEQgSEQPVHLIYGVTRDADLVEVER 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 255 LTELRRRVGRLEVHVVVARPDPDWDgRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFVA 334
Cdd:NF040810  254 LEAFAARLPNFTFRTCVADAASAHP-RKGYVTQHIEAEWLNDGDVDVYLCGPPPMVDAVRGWFREQGITPASFHYEKFTP 332


                  .
gi 2522989786 335 S 335
Cdd:NF040810  333 S 333
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 5-332 2.93e-50

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 181.98  E-value: 2.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   5 QVTVgysDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQ-SGICGTCVATCTAGRYQMGRTE--GLSDVERAARKILTCQT 81
Cdd:COG2871    36 KITI---NGDGKEIEVEEGQTLLDALLRQGIFLPSACGgGGTCGQCKVKVLEGGGDILPTEtfHLSDRERKEGYRLACQV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  82 FVTSDCRIELqypvdDNAALLVTG-DGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQVPG------------- 147
Cdd:COG2871   113 KVKSDMEIEV-----PEEVFGVKKwEATVVSNENVTTFIKELVLELPE-GEEIDFKAGQYIQIEVPPyevdfkdfdipee 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 148 ----------TNVWRNYSYA-HPADGrGECEFIIRL------LPDGVMSNYLRDRaQPGDHIALRCSKGSFYLRPIVRPV 210
Cdd:COG2871   187 ekfglfdkndEEVTRAYSMAnYPAEK-GIIELNIRIatppmdVPPGIGSSYIFSL-KPGDKVTISGPYGEFFLRDSDREM 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQSLDADVAH--PVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPD--WDGRTGLVT 286
Cdd:COG2871   265 VFIGGGAGMAPLRSHIFDLLERGKTdrKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEdnWDGETGFIH 344

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2522989786 287 DLLDERMLASGDA----DVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:COG2871   345 EVLYENYLKDHPApedcEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDF 394
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
106-201 2.79e-29

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 111.90  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 106 DGVVTAVELVSPSTAILRVDTSGMAGALRYRAGQ--FAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLr 183
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQhlFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYL- 79

                          90
                  ....*....|....*...
gi 2522989786 184 DRAQPGDHIALRCSKGSF 201
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRF 97
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-91 3.56e-23

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.14  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   1 MAvrQVTVgysDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQ 80
Cdd:COG0633     1 MP--KVTF---IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQ 75

                          90
                  ....*....|.
gi 2522989786  81 TFVTSDCRIEL 91
Cdd:COG0633    76 ARPTSDLVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 13-90 4.76e-21

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 87.84  E-value: 4.76e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2522989786  13 GTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSDCRIE 90
Cdd:cd00207     7 GSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGLVIE 84
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-84 3.65e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 65.24  E-value: 3.65e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786  12 DGTHKTMPVRCDQT-VLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEgLSDVERAARK-ILTCQTFVT 84
Cdd:pfam00111   4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSF-LEDDELAAGYvVLACQTYPK 77
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 2-90 7.21e-12

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 62.47  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   2 AVRQVTVGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQT 81
Cdd:TIGR02008   1 ATYKVTLVNPDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVA 80


                  ....*....
gi 2522989786  82 FVTSDCRIE 90
Cdd:TIGR02008  81 YPTSDCTIE 89
petF CHL00134
ferredoxin; Validated
 1-89 2.53e-10

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 57.81  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   1 MAVRQVT-VGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTC 79
Cdd:CHL00134    1 MATYKVTlLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTC 80

                          90
                  ....*....|
gi 2522989786  80 QTFVTSDCRI 89
Cdd:CHL00134   81 VAYPTSDCTI 90
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 364-551 1.16e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 41.85  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 364 AVVIGGSIAGIAAAKMLSETFDRVIVLEKDgPHRRREGRPGAaqgwhLHHlltAGQIELERIfpGIVDDMVREGAfkVDM 443
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERA-PPPRPDGRGIA-----LSP---RSLELLRRL--GLWDRLLARGA--PIR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 444 AAQYRIRLGGTWKK----PGTSDIEIVCAGRPLLEWCVRRRLDDEPrIDFRYESEVADLAFDRAnnaivGVAVDNGDAdg 519
Cdd:COG0654    73 GIRVRDGSDGRVLArfdaAETGLPAGLVVPRADLERALLEAARALG-VELRFGTEVTGLEQDAD-----GVTVTLADG-- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2522989786 520 gdglQVVPAEFVVDASGKNTRVPEFLERLGVG 551
Cdd:COG0654   145 ----RTLRADLVVGADGARSAVRRLLGIGFTG 172
PLN02268 PLN02268
probable polyamine oxidase
 363-391 2.17e-03

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 41.21  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 2522989786 363 TAVVIGGSIAGIAAAKMLSETFDRVIVLE 391
Cdd:PLN02268    2 SVIVIGGGIAGIAAARALHDASFKVTLLE 30
 
Name Accession Description Interval E-value
BenDO_FAD_NAD cd06209
Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons ...
 104-333 7.25e-111

Benzoate dioxygenase reductase (BenDO) FAD/NAD binding domain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. As a Class I bacterial dioxygenases, benzoate dioxygenase like proteins combine an [2Fe-2S] cluster containing N-terminal ferredoxin at the end fused to an FAD/NADP(P) domain. In dioxygenase FAD/NAD(P) binding domain, the reductase transfers 2 electrons from NAD(P)H to the oxygenase which insert into an aromatic substrate, an initial step in microbial aerobic degradation of aromatic rings. Flavin oxidoreductases use flavins as substrates, unlike flavoenzymes which have a flavin prosthetic group.


Pssm-ID: 99805 [Multi-domain]  Cd Length: 228  Bit Score: 338.03  E-value: 7.25e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 104 TGDGVVTAVELVSPSTAILRVDTSGMaGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRgECEFIIRLLPDGVMSNYLR 183
Cdd:cd06209     1 TFEATVTEVERLSDSTIGLTLELDEA-GALAFLPGQYVNLQVPGTDETRSYSFSSAPGDP-RLEFLIRLLPGGAMSSYLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADV-AHPVYLLYGVERTEDLCKLDELTELRRRV 262
Cdd:cd06209    79 DRAQPGDRLTLTGPLGSFYLREVKRPLLMLAGGTGLAPFLSMLDVLAEDGsAHPVHLVYGVTRDADLVELDRLEALAERL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 263 GRLEVHVVVARPDPdWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06209   159 PGFSFRTVVADPDS-WHPRKGYVTDHLEAEDLNDGDVDVYLCGPPPMVDAVRSWLDEQGIEPANFYYEKFT 228
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
5-337 2.75e-104

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 325.55  E-value: 2.75e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   5 QVTVGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRT--EGLSDVERAARKILTCQTF 82
Cdd:PRK11872    4 KVALSFADGKTLFFPVGKDELLLDAALRNGINLPLDCREGVCGTCQGRCESGIYSQDYVdeDALSERDLAQRKMLACQTR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  83 VTSDCRIELQYPVD-DNAALLVTGDGVVTAVELVSPSTAILRVDTSGMAGALRYRAGQFAQLQVPGTNVWRNYSYAHPAD 161
Cdd:PRK11872   84 VKSDAAFYFDFDSSlCNAGDTLKISGVVTAVELVSETTAILHLDASAHGRQLDFLPGQYARLQIPGTDDWRSYSFANRPN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 162 GRGECEFIIRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSL-DADVAHPVYLL 240
Cdd:PRK11872  164 ATNQLQFLIRLLPDGVMSNYLRERCQVGDEILFEAPLGAFYLREVERPLVFVAGGTGLSAFLGMLDELaEQGCSPPVHLY 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 241 YGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHN 320
Cdd:PRK11872  244 YGVRHAADLCELQRLAAYAERLPNFRYHPVVSKASADWQGKRGYIHEHFDKAQLRDQAFDMYLCGPPPMVEAVKQWLDEQ 323

                         330
                  ....*....|....*..
gi 2522989786 321 GFHRVGLYYEKFVASGA 337
Cdd:PRK11872  324 ALENYRLYYEKFTQSNT 340
BenC NF040810
benzoate 1,2-dioxygenase electron transfer component BenC;
23-335 6.18e-92

benzoate 1,2-dioxygenase electron transfer component BenC;


Pssm-ID: 468751 [Multi-domain]  Cd Length: 333  Bit Score: 292.50  E-value: 6.18e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  23 DQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRT---EGLSDVERAARKILTCQTFVTSDCRIELQYPvddnA 99
Cdd:NF040810   20 GETVLDAAYRQKINIPMDCRDGACGTCKCRCESGSYDLGDDyieDALTEEEAAQGYVLTCQMVPQSDCVIRVPAS----S 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 100 ALLVTG----DGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQVPGTNVWRNYSYAHPAdGRGECEFIIRLLPD 175
Cdd:NF040810   96 AACKTGqatfEATVAAVEQLSDSTIELSLDLDD-DAALAFLPGQYVNIQVPGTGQTRSYSFSSLP-GAREASFLIRNVPG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 176 GVMSNYLRDRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDAD-VAHPVYLLYGVERTEDLCKLDE 254
Cdd:NF040810  174 GLMSSYLTERAKPGDRLSLTGPLGSFYLREVTRPLLMLAGGTGLAPFLSMLEVLAEQgSEQPVHLIYGVTRDADLVEVER 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 255 LTELRRRVGRLEVHVVVARPDPDWDgRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFVA 334
Cdd:NF040810  254 LEAFAARLPNFTFRTCVADAASAHP-RKGYVTQHIEAEWLNDGDVDVYLCGPPPMVDAVRGWFREQGITPASFHYEKFTP 332


                  .
gi 2522989786 335 S 335
Cdd:NF040810  333 S 333
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 109-332 7.99e-57

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 194.35  E-value: 7.99e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDtsgMAGALRYRAGQFAQLQVPGT-NVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDRAQ 187
Cdd:cd06187     1 VVSVERLTHDIAVVRLQ---LDQPLPFWAGQYVNVTVPGRpRTWRAYSPANPPNEDGEIEFHVRAVPGGRVSNALHDELK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 188 PGDHIALRCSKGSFYLRPIV-RPVILVAGGTGLSAILAMAQSLDA-DVAHPVYLLYGVERTEDLCKLDELTELRRRVGRL 265
Cdd:cd06187    78 VGDRVRLSGPYGTFYLRRDHdRPVLCIAGGTGLAPLRAIVEDALRrGEPRPVHLFFGARTERDLYDLEGLLALAARHPWL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2522989786 266 EVHVVVARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06187   158 RVVPVVSHEEGAWTGRRGLVTDVVGRDGPDWADHDIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 107-333 2.91e-55

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 190.63  E-value: 2.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 107 GVVTAVELVSPSTAILRV---DTSGMAGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLR 183
Cdd:cd06210     4 AEIVAVDRVSSNVVRLRLqpdDAEGAGIAAEFVPGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLPGGAFSTYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DRAQPGDHIALRCSKGSFYLRPI-VRPVILVAGGTGLSAILAMAQSL-DADVAHPVYLLYGVERTEDLCKLDELTELRRR 261
Cdd:cd06210    84 TRAKVGQRLNLRGPLGAFGLRENgLRPRWFVAGGTGLAPLLSMLRRMaEWGEPQEARLFFGVNTEAELFYLDELKRLADS 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2522989786 262 VGRLEVHVVVARPDPDWDGRTGLVTDLLDERmLASGDA--DVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06210   164 LPNLTVRICVWRPGGEWEGYRGTVVDALRED-LASSDAkpDIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKFL 236
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 5-332 2.93e-50

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 181.98  E-value: 2.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   5 QVTVgysDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQ-SGICGTCVATCTAGRYQMGRTE--GLSDVERAARKILTCQT 81
Cdd:COG2871    36 KITI---NGDGKEIEVEEGQTLLDALLRQGIFLPSACGgGGTCGQCKVKVLEGGGDILPTEtfHLSDRERKEGYRLACQV 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  82 FVTSDCRIELqypvdDNAALLVTG-DGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQVPG------------- 147
Cdd:COG2871   113 KVKSDMEIEV-----PEEVFGVKKwEATVVSNENVTTFIKELVLELPE-GEEIDFKAGQYIQIEVPPyevdfkdfdipee 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 148 ----------TNVWRNYSYA-HPADGrGECEFIIRL------LPDGVMSNYLRDRaQPGDHIALRCSKGSFYLRPIVRPV 210
Cdd:COG2871   187 ekfglfdkndEEVTRAYSMAnYPAEK-GIIELNIRIatppmdVPPGIGSSYIFSL-KPGDKVTISGPYGEFFLRDSDREM 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQSLDADVAH--PVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPD--WDGRTGLVT 286
Cdd:COG2871   265 VFIGGGAGMAPLRSHIFDLLERGKTdrKITFWYGARSLRELFYLEEFRELEKEHPNFKFHPALSEPLPEdnWDGETGFIH 344

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2522989786 287 DLLDERMLASGDA----DVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:COG2871   345 EVLYENYLKDHPApedcEAYLCGPPPMIDAVIKMLDDLGVEEENIYFDDF 394
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 106-332 4.02e-50

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 175.96  E-value: 4.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 106 DGVVTAVELVSPStaILRVDTSgMAGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDR 185
Cdd:cd06213     2 RGTIVAQERLTHD--IVRLTVQ-LDRPIAYKAGQYAELTLPGLPAARSYSFANAPQGDGQLSFHIRKVPGGAFSGWLFGA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 186 AQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAM-AQSLDADVAHPVYLLYGVERTEDLCKLDELTELRRR-VG 263
Cdd:cd06213    79 DRTGERLTVRGPFGDFWLRPGDAPILCIAGGSGLAPILAIlEQARAAGTKRDVTLLFGARTQRDLYALDEIAAIAARwRG 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 264 RLE-VHVVVARP-DPDWDGRTGLVTDLLDERMLASGDAdvYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06213   159 RFRfIPVLSEEPaDSSWKGARGLVTEHIAEVLLAATEA--YLCGPPAMIDAAIAVLRALGIAREHIHADRF 227
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
106-331 3.78e-48

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 170.36  E-value: 3.78e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 106 DGVVTAVELVSPSTAILRVDTSGMAGALRYRAGQFAQLQVP--GTNVWRNYSYAHPADgRGECEFIIRLLPDGVMSNYLR 183
Cdd:COG1018     5 PLRVVEVRRETPDVVSFTLEPPDGAPLPRFRPGQFVTLRLPidGKPLRRAYSLSSAPG-DGRLEITVKRVPGGGGSNWLH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DRAQPGDHIALRCSKGSFYLRPIV-RPVILVAGGTGLSAILAMAQSL-DADVAHPVYLLYGVERTEDLCKLDELTELRRR 261
Cdd:COG1018    84 DHLKVGDTLEVSGPRGDFVLDPEPaRPLLLIAGGIGITPFLSMLRTLlARGPFRPVTLVYGARSPADLAFRDELEALAAR 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 262 VGRLEVHVVVARPDPDWDGRtgLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEK 331
Cdd:COG1018   164 HPRLRLHPVLSREPAGLQGR--LDAELLAALLPDPADAHVYLCGPPPMMEAVRAALAELGVPEERIHFER 231
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 105-333 6.84e-47

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 167.12  E-value: 6.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 105 GDGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRD 184
Cdd:cd06212     1 FVGTVVAVEALTHDIRRLRLRLEE-PEPIKFFAGQYVDITVPGTEETRSFSMANTPADPGRLEFIIKKYPGGLFSSFLDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 185 RAQPGDHIALRCSKGSFYLR-PIVRPVILVAGGTGLSAILAMAQSLDAD-VAHPVYLLYGVERTEDLCKLDELTELRRRV 262
Cdd:cd06212    80 GLAVGDPVTVTGPYGTCTLReSRDRPIVLIGGGSGMAPLLSLLRDMAASgSDRPVRFFYGARTARDLFYLEEIAALGEKI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2522989786 263 GRLEVHVVVARPDPD--WDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06212   160 PDFTFIPALSESPDDegWSGETGLVTEVVQRNEATLAGCDVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKFT 232
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 109-330 5.65e-46

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 165.04  E-value: 5.65e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSgmAGALRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLpdGVMSNYLRdRAQP 188
Cdd:COG0543     2 VVSVERLAPDVYLLRLEAP--LIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVV--GKGTRALA-ELKP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 189 GDHIALRCSKGSFY-LRPIVRPVILVAGGTGLSAILAMAQSLDADvAHPVYLLYGVERTEDLCKLDELtelrRRVGRLEV 267
Cdd:COG0543    77 GDELDVRGPLGNGFpLEDSGRPVLLVAGGTGLAPLRSLAEALLAR-GRRVTLYLGARTPEDLYLLDEL----EALADFRV 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2522989786 268 HVVVarpDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYE 330
Cdd:COG0543   152 VVTT---DDGWYGRKGFVTDALKELLAEDSGDDVYACGPPPMMKAVAELLLERGVPPERIYVS 211
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 109-333 1.98e-44

Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.


Pssm-ID: 99787  Cd Length: 232  Bit Score: 160.11  E-value: 1.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGMAgalRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDRAQP 188
Cdd:cd06190     1 LVDVRELTHDVAEFRFALDGPA---DFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKPGGAASNALFDNLEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 189 GDHIALRCSKGSFYLRP-IVRPVILVAGGTGLSAILAMAQSLDADVA---HPVYLLYGVERTEDLCKLDELTELRRRVGR 264
Cdd:cd06190    78 GDELELDGPYGLAYLRPdEDRDIVCIAGGSGLAPMLSILRGAARSPYlsdRPVDLFYGGRTPSDLCALDELSALVALGAR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2522989786 265 LEVHVVV----ARPDPDWDGRTGLVTDLLDERMLAS-GDADVYLCGPVAMVDAARTWLDHNgfHRVG---LYYEKFV 333
Cdd:cd06190   158 LRVTPAVsdagSGSAAGWDGPTGFVHEVVEATLGDRlAEFEFYFAGPPPMVDAVQRMLMIE--GVVPfdqIHFDRFV 232
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 110-321 8.14e-40

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 146.82  E-value: 8.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 110 TAVELVSPSTAILRVDTSGmagALRYRAGQFAQLQVP--GTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDrAQ 187
Cdd:cd00322     1 VATEDVTDDVRLFRLQLPN---GFSFKPGQYVDLHLPgdGRGLRRAYSIASSPDEEGELELTVKIVPGGPFSAWLHD-LK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 188 PGDHIALRCSKGSFYL-RPIVRPVILVAGGTGLSAILAMAQSLDADVA-HPVYLLYGVERTEDLCKLDELTELRRRVGRL 265
Cdd:cd00322    77 PGDEVEVSGPGGDFFLpLEESGPVVLIAGGIGITPFRSMLRHLAADKPgGEITLLYGARTPADLLFLDELEELAKEGPNF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2522989786 266 EVHVVVARPDPD--WDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNG 321
Cdd:cd00322   157 RLVLALSRESEAklGPGGRIDREAEILALLPDDSGALVYICGPPAMAKAVREALVSLG 214
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 109-322 7.47e-38

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 141.15  E-value: 7.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTA--ILRVDtsgmaGALRYRAGQFAQLQVPGtNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDRA 186
Cdd:cd06189     3 VESIEPLNDDVYrvRLKPP-----APLDFLAGQYLDLLLDD-GDKRPFSIASAPHEDGEIELHIRAVPGGSFSDYVFEEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 187 QPGDHIALRCSKGSFYLRP-IVRPVILVAGGTGLSAILAMAQSLDA-DVAHPVYLLYGVERTEDLCKLDELTELRRRVGR 264
Cdd:cd06189    77 KENGLVRIEGPLGDFFLREdSDRPLILIAGGTGFAPIKSILEHLLAqGSKRPIHLYWGARTEEDLYLDELLEAWAEAHPN 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2522989786 265 LEVHVVVARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGF 322
Cdd:cd06189   157 FTYVPVLSEPEEGWQGRTGLVHEAVLEDFPDLSDFDVYACGSPEMVYAARDDFVEKGL 214
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 105-332 1.33e-36

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 137.78  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 105 GDGVVTAVELVSPSTAILRVDTSGmAGALRYRAGQFAQLQV---PGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNY 181
Cdd:cd06217     2 RVLRVTEIIQETPTVKTFRLAVPD-GVPPPFLAGQHVDLRLtaiDGYTAQRSYSIASSPTQRGRVELTVKRVPGGEVSPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 182 LRDRAQPGDHIALRCSKGSFYLRPI-VRPVILVAGGTGLSAILAMAQSL-DADVAHPVYLLYGVERTEDLCKLDELTELR 259
Cdd:cd06217    81 LHDEVKVGDLLEVRGPIGTFTWNPLhGDPVVLLAGGSGIVPLMSMIRYRrDLGWPVPFRLLYSARTAEDVIFRDELEQLA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786 260 RRVGRLEVHVVVARP-DPDWDGRTGLVT-DLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06217   161 RRHPNLHVTEALTRAaPADWLGPAGRITaDLIAELVPPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 23-334 2.21e-36

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 140.39  E-value: 2.21e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  23 DQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTE--GLSDVERAARKILTCQTFVTSDCRIELQYpvddnaa 100
Cdd:PRK07609   19 DETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEQGPHQasALSGEERAAGEALTCCAKPLSDLVLEARE------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 101 llVTGDGV---------VTAVELVSPSTAILRVDTSgmAGA-LRYRAGQFAQLQVPGtNVWRNYSYAHPADGRGECEFII 170
Cdd:PRK07609   92 --VPALGDipvkklpcrVASLERVAGDVMRLKLRLP--ATErLQYLAGQYIEFILKD-GKRRSYSIANAPHSGGPLELHI 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 171 RLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIV-RPVILVAGGTGLSAILAMAQSLDA-DVAHPVYLLYGVERTED 248
Cdd:PRK07609  167 RHMPGGVFTDHVFGALKERDILRIEGPLGTFFLREDSdKPIVLLASGTGFAPIKSIVEHLRAkGIQRPVTLYWGARRPED 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 249 LcKLDELTELR-RRVGRLEVHVVV--ARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAArtwldHNGFHRV 325
Cdd:PRK07609  247 L-YLSALAEQWaEELPNFRYVPVVsdALDDDAWTGRTGFVHQAVLEDFPDLSGHQVYACGSPVMVYAA-----RDDFVAA 320


                  ....*....
gi 2522989786 326 GLYYEKFVA 334
Cdd:PRK07609  321 GLPAEEFFA 329
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 106-332 4.78e-36

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 136.30  E-value: 4.78e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 106 DGVVTAVELVSPSTAILRVDTSGMAGaLRYRAGQFAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDR 185
Cdd:cd06211     8 EGTVVEIEDLTPTIKGVRLKLDEPEE-IEFQAGQYVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLVPGGIATTYVHKQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 186 AQPGDHIALRCSKGSFYLRPI-VRPVILVAGGTGLSAILAM-AQSLDADVAHPVYLLYGVERTEDLCKLDELTELRRRVG 263
Cdd:cd06211    87 LKEGDELEISGPYGDFFVRDSdQRPIIFIAGGSGLSSPRSMiLDLLERGDTRKITLFFGARTRAELYYLDEFEALEKDHP 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786 264 RLEVHVVVAR--PDPDWDGRTGLVTDLL----DERMlasGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06211   167 NFKYVPALSRepPESNWKGFTGFVHDAAkkhfKNDF---RGHKAYLCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 109-332 3.48e-35

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 133.89  E-value: 3.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGmaGALRYRAGQFAQLQVP--GTNVWRNYSYAHPADGRGEC-EFIIRLLPDGVMSNYLRDR 185
Cdd:cd06216    22 VVAVRPETADMVTLTLRPNR--GWPGHRAGQHVRLGVEidGVRHWRSYSLSSSPTQEDGTiTLTVKAQPDGLVSNWLVNH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 186 AQPGDHIALRCSKGSFYL-RPIVRPVILVAGGTGLSAILAMAQSLDA-DVAHPVYLLYGVERTEDLCKLDELTELRRRVG 263
Cdd:cd06216   100 LAPGDVVELSQPQGDFVLpDPLPPRLLLIAAGSGITPVMSMLRTLLArGPTADVVLLYYARTREDVIFADELRALAAQHP 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2522989786 264 RLEVHVVVARPDPDwdGRTGLvtDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGfHRVGLYYEKF 332
Cdd:cd06216   180 NLRLHLLYTREELD--GRLSA--AHLDAVVPDLADRQVYACGPPGFLDAAEELLEAAG-LADRLHTERF 243
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 108-322 4.37e-32

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 124.98  E-value: 4.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 108 VVTAVELVSPSTAILRVDTSGMagaLRYRAGQFAQLQVP---GTNVWRNYSYA-HPADGrgECEFIIRLLPDGVMSNYLR 183
Cdd:cd06195     1 TVLKRRDWTDDLFSFRVTRDIP---FRFQAGQFTKLGLPnddGKLVRRAYSIAsAPYEE--NLEFYIILVPDGPLTPRLF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 dRAQPGDHIALRC-SKGSFYLRPIVRP--VILVAGGTGLSAILAMAQslDADVAHP---VYLLYGVERTEDLCKLDELTE 257
Cdd:cd06195    76 -KLKPGDTIYVGKkPTGFLTLDEVPPGkrLWLLATGTGIAPFLSMLR--DLEIWERfdkIVLVHGVRYAEELAYQDEIEA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2522989786 258 LRRRV-GRLEVHVVVARPDPDWdGRTGLVTDLLDERMLA--------SGDADVYLCGPVAMVDAARTWLDHNGF 322
Cdd:cd06195   153 LAKQYnGKFRYVPIVSREKENG-ALTGRIPDLIESGELEehaglpldPETSHVMLCGNPQMIDDTQELLKEKGF 225
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 130-333 3.56e-31

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 122.27  E-value: 3.56e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 130 AGALRYRAGQFAQLQVP--GTNVWRNYSYAHPADgRGECEFIIRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIV 207
Cdd:cd06214    28 RDAFRYRPGQFLTLRVPidGEEVRRSYSICSSPG-DDELRITVKRVPGGRFSNWANDELKAGDTLEVMPPAGRFTLPPLP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 208 --RPVILVAGGTGLSAILAMAQS-LDADVAHPVYLLYGVERTEDLCKLDELTELRRR-VGRLEVHVVVARPDPDWDGRTG 283
Cdd:cd06214   107 gaRHYVLFAAGSGITPVLSILKTaLAREPASRVTLVYGNRTEASVIFREELADLKARyPDRLTVIHVLSREQGDPDLLRG 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786 284 -----LVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06214   187 rldaaKLNALLKNLLDATEFDEAFLCGPEPMMDAVEAALLELGVPAERIHRELFT 241
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
106-201 2.79e-29

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 111.90  E-value: 2.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 106 DGVVTAVELVSPSTAILRVDTSGMAGALRYRAGQ--FAQLQVPGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLr 183
Cdd:pfam00970   1 PLTLVEKELVSHDTRIFRFALPHPDQVLGLPVGQhlFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYPGGKMSQYL- 79

                          90
                  ....*....|....*...
gi 2522989786 184 DRAQPGDHIALRCSKGSF 201
Cdd:pfam00970  80 DELKIGDTIDFKGPLGRF 97
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 109-333 2.25e-27

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 110.82  E-value: 2.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGmagALRYRAGQFAQLQVPGTnVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDRAQP 188
Cdd:cd06194     1 VVSLQRLSPDVLRVRLEPDR---PLPYLPGQYVNLRRAGG-LARSYSPTSLPDGDNELEFHIRRKPNGAFSGWLGEEARP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 189 GDHIALRCSKGSFYLRPIV--RPVILVAGGTGLSAILAMAQS-LDADVAHPVYLLYGVERTEDLCKLDELTELRRRVGRL 265
Cdd:cd06194    77 GHALRLQGPFGQAFYRPEYgeGPLLLVGAGTGLAPLWGIARAaLRQGHQGEIRLVHGARDPDDLYLHPALLWLAREHPNF 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2522989786 266 EVHVVVAR-PDPDWDGRTGLVTdlLDERMLASGDAdVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06194   157 RYIPCVSEgSQGDPRVRAGRIA--AHLPPLTRDDV-VYLCGAPSMVNAVRRRAFLAGAPMKRIYADPFE 222
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 132-333 2.73e-27

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 110.42  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 132 ALRYRAGQFAQLQVPGTNVWRnysyAHP------ADGRGECEFIIRLLPDGvmSNYLRDRAQPGDHIALRCSKGSFYLRP 205
Cdd:cd06198    20 ALGHRAGQFAFLRFDASGWEE----PHPftissaPDPDGRLRFTIKALGDY--TRRLAERLKPGTRVTVEGPYGRFTFDD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 206 IVRPVILVAGGTGLSAILAMAQSL-DADVAHPVYLLYGVERTEDLCKLDELTELRRRVGRlEVHVVVARPDPdWDGRTGL 284
Cdd:cd06198    94 RRARQIWIAGGIGITPFLALLEALaARGDARPVTLFYCVRDPEDAVFLDELRALAAAAGV-VLHVIDSPSDG-RLTLEQL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2522989786 285 VTDLLDERmlasGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKFV 333
Cdd:cd06198   172 VRALVPDL----ADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
107-332 8.15e-27

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 114.61  E-value: 8.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 107 GVVTAVELVSPSTAILRVdTSGMAGALRYRAGQFAQLQVPGTNVWRNysyAHP------ADGRGECEFIIRLLPDGvmSN 180
Cdd:COG4097   217 YRVESVEPEAGDVVELTL-RPEGGRWLGHRAGQFAFLRFDGSPFWEE---AHPfsissaPGGDGRLRFTIKALGDF--TR 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 181 YLRdRAQPGDHIALRCSKGSFYL--RPIVRPVILVAGGTGLSAILAMAQSLDADVAH--PVYLLYGVERTEDLCKLDELT 256
Cdd:COG4097   291 RLG-RLKPGTRVYVEGPYGRFTFdrRDTAPRQVWIAGGIGITPFLALLRALAARPGDqrPVDLFYCVRDEEDAPFLEELR 369

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2522989786 257 ELRRRVGRLEVHVVVarpdpdwDGRTGLVT-DLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:COG4097   370 ALAARLAGLRLHLVV-------SDEDGRLTaERLRRLVPDLAEADVFFCGPPGMMDALRRDLRALGVPARRIHQERF 439
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 109-322 2.05e-26

Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.


Pssm-ID: 99817 [Multi-domain]  Cd Length: 253  Bit Score: 108.85  E-value: 2.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAI--LRVDtSGMAGALRYRAGQFAQLQVPG----TnvwrnYSYAHPADGRGECEFIIRLLpdGVMSNYL 182
Cdd:cd06221     1 IVEVVDETEDIKTftLRLE-DDDEELFTFKPGQFVMLSLPGvgeaP-----ISISSDPTRRGPLELTIRRV--GRVTEAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 183 rDRAQPGDHIALRCSKGSFYLRPIVR--PVILVAGGTGLSAILAMAQSLDADVAH--PVYLLYGVERTEDLCKLDELTEL 258
Cdd:cd06221    73 -HELKPGDTVGLRGPFGNGFPVEEMKgkDLLLVAGGLGLAPLRSLINYILDNREDygKVTLLYGARTPEDLLFKEELKEW 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2522989786 259 RRRVGrLEVHVVVARPDPDWDGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNGF 322
Cdd:cd06221   152 AKRSD-VEVILTVDRAEEGWTGNVGLVTDLLPELTLDPDNTVAIVCGPPIMMRFVAKELLKLGV 214
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 135-332 3.18e-26

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 108.41  E-value: 3.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 135 YRAGQF--AQLQVPGTNVW--RNYSYAhpaDGRGECEFII--RLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIV- 207
Cdd:cd06184    37 FLPGQYlsVRVKLPGLGYRqiRQYSLS---DAPNGDYYRIsvKREPGGLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASd 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 208 RPVILVAGGTGLSAILAMAQSL-DADVAHPVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDWDGRTGLVT 286
Cdd:cd06184   114 RPLVLISAGVGITPMLSMLEALaAEGPGRPVTFIHAARNSAVHAFRDELEELAARLPNLKLHVFYSEPEAGDREEDYDHA 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2522989786 287 DLLD----ERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06184   194 GRIDlallRELLLPADADFYLCGPVPFMQAVREGLKALGVPAERIHYEVF 243
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 109-313 5.99e-26

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 107.27  E-value: 5.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGMAGALRYRAGQFAQLQVP--GTNVWRNYS-YAHPADgRGECEFIIRLLPDGVMSNYLrDR 185
Cdd:cd06183     3 LVSKEDISHDTRIFRFELPSPDQVLGLPVGQHVELKAPddGEQVVRPYTpISPDDD-KGYFDLLIKIYPGGKMSQYL-HS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 186 AQPGDHIALRCSKGSFYLRP--IVRPVILVAGGTGLSAILAMAQSLDADVAHP--VYLLYGVERTED-LCKlDELTELRR 260
Cdd:cd06183    81 LKPGDTVEIRGPFGKFEYKPngKVKHIGMIAGGTGITPMLQLIRAILKDPEDKtkISLLYANRTEEDiLLR-EELDELAK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2522989786 261 RV-GRLEVHVVVARPDPDWDGRTGLVT-DLLDERMLASGDADVY--LCGPVAMVDAA 313
Cdd:cd06183   160 KHpDRFKVHYVLSRPPEGWKGGVGFITkEMIKEHLPPPPSEDTLvlVCGPPPMIEGA 216
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 134-332 4.25e-25

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 104.59  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 134 RYRAGQFAQLQV--PGTNVWRNYSYAHPADGRGECEFIIRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIV-RPV 210
Cdd:cd06215    27 AYKPGQFLTLELeiDGETVYRAYTLSSSPSRPDSLSITVKRVPGGLVSNWLHDNLKVGDELWASGPAGEFTLIDHPaDKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQSL-----DADVAhpvyLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPD-WDGRTGl 284
Cdd:cd06215   107 LLLSAGSGITPMMSMARWLldtrpDADIV----FIHSARSPADIIFADELEELARRHPNFRLHLILEQPAPGaWGGYRG- 181

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2522989786 285 vtdLLDERMLAS-----GDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06215   182 ---RLNAELLALlvpdlKERTVFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 134-332 3.38e-24

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 101.83  E-value: 3.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 134 RYRAGQFAQLQVP--GTNVWRNYSYAHPAdGRGECEFIIRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPI-VRPV 210
Cdd:cd06191    27 GFRPGQHVTLKLDfdGEELRRCYSLCSSP-APDEISITVKRVPGGRVSNYLREHIQPGMTVEVMGPQGHFVYQPQpPGRY 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQS-LDADVAHPVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDWDgrTGLVTDLL 289
Cdd:cd06191   106 LLVAAGSGITPLMAMIRAtLQTAPESDFTLIHSARTPADMIFAQELRELADKPQRLRLLCIFTRETLDSD--LLHGRIDG 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2522989786 290 DERMLASGDAD-----VYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:cd06191   184 EQSLGAALIPDrlereAFICGPAGMMDAVETALKELGMPPERIHTERF 231
Fdx COG0633
Ferredoxin [Energy production and conversion];
1-91 3.56e-23

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 94.14  E-value: 3.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   1 MAvrQVTVgysDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQ 80
Cdd:COG0633     1 MP--KVTF---IPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDEERAAGSRLACQ 75

                          90
                  ....*....|.
gi 2522989786  81 TFVTSDCRIEL 91
Cdd:COG0633    76 ARPTSDLVVEL 86
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 13-90 4.76e-21

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 87.84  E-value: 4.76e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2522989786  13 GTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSDCRIE 90
Cdd:cd00207     7 GSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEEAEGGYVLACQTRVTDGLVIE 84
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 212-314 4.79e-21

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 88.86  E-value: 4.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 212 LVAGGTGLSAILAMAQSL--DADVAHPVYLLYGVERTEDLCKLDELTELRRRV-GRLEVHVVVARPDPDWDGRTGLVTDL 288
Cdd:pfam00175   1 MIAGGTGIAPVRSMLRAIleDPKDPTQVVLVFGNRNEDDILYREELDELAEKHpGRLTVVYVVSRPEAGWTGGKGRVQDA 80

                          90       100
                  ....*....|....*....|....*...
gi 2522989786 289 LDERML--ASGDADVYLCGPVAMVDAAR 314
Cdd:pfam00175  81 LLEDHLslPDEETHVYVCGPPGMIKAVR 108
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 135-332 2.01e-20

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 92.37  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 135 YRAGQFAQLQVPGTNV--------------W-----------------RNYSYA-HPADGrGECEFIIRLL--------- 173
Cdd:cd06188    39 FKAGGYIQIEIPAYEIayadfdvaekyradWdkfglwqlvfkhdepvsRAYSLAnYPAEE-GELKLNVRIAtpppgnsdi 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 174 PDGVMSNYLRDRaQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADV--AHPVYLLYGVERTEDLCK 251
Cdd:cd06188   118 PPGIGSSYIFNL-KPGDKVTASGPFGEFFIKDTDREMVFIGGGAGMAPLRSHIFHLLKTLksKRKISFWYGARSLKELFY 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 252 LDELTELRRRVGRLEVHVVVARPDP--DWDGRTGLVTDLL----DERMLASGDADVYLCGPVAMVDAARTWLDHNGFHRV 325
Cdd:cd06188   197 QEEFEALEKEFPNFKYHPVLSEPQPedNWDGYTGFIHQVLlenyLKKHPAPEDIEFYLCGPPPMNSAVIKMLDDLGVPRE 276


                  ....*..
gi 2522989786 326 GLYYEKF 332
Cdd:cd06188   277 NIAFDDF 283
PRK13289 PRK13289
NO-inducible flavohemoprotein;
133-332 8.66e-19

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 89.47  E-value: 8.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 133 LRYRAGQF--AQLQVPGTNV--WRNYSYAHPADGRG-------EcefiirllPDGVMSNYLRDRAQPGDHIALRCSKGSF 201
Cdd:PRK13289  183 ADFKPGQYlgVRLDPEGEEYqeIRQYSLSDAPNGKYyrisvkrE--------AGGKVSNYLHDHVNVGDVLELAAPAGDF 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 202 YLRPIV-RPVILVAGGTGLSAILAMAQSLDA-DVAHPVYLLYGVE-------RtedlcklDELTELRRRVGRLEVHVVVA 272
Cdd:PRK13289  255 FLDVASdTPVVLISGGVGITPMLSMLETLAAqQPKRPVHFIHAARnggvhafR-------DEVEALAARHPNLKAHTWYR 327

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2522989786 273 RPDP-DWDGR----TGLVT-DLLDErMLASGDADVYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:PRK13289  328 EPTEqDRAGEdfdsEGLMDlEWLEA-WLPDPDADFYFCGPVPFMQFVAKQLLELGVPEERIHYEFF 392
fre PRK08051
FMN reductase; Validated
 208-320 5.72e-16

FMN reductase; Validated


Pssm-ID: 236142 [Multi-domain]  Cd Length: 232  Bit Score: 77.97  E-value: 5.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 208 RPVILVAGGTGLSAILAMAQS-LDADVAHPVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDWDGRTGLVT 286
Cdd:PRK08051  103 RPLLLIAGGTGFSYARSILLTaLAQGPNRPITLYWGGREEDHLYDLDELEALALKHPNLHFVPVVEQPEEGWQGKTGTVL 182

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2522989786 287 D--LLDERMLAsgDADVYLCGPVAMVDAARTWLDHN 320
Cdd:PRK08051  183 TavMQDFGSLA--EYDIYIAGRFEMAKIARELFCRE 216
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 109-315 2.72e-14

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 72.52  E-value: 2.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRvdtsgmagalRYRAGQFAQLQVPGtNVWRNYSYAHPADGRGECEFIIRLLPD---GvmSNYLRDR 185
Cdd:cd06185    10 IRSFELEAPDGAPLP----------AFEPGAHIDVHLPN-GLVRQYSLCGDPADRDRYRIAVLREPAsrgG--SRYMHEL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 186 AQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADVAhPVYLLYGVERTEDLCKLDELTELRRrvGRL 265
Cdd:cd06185    77 LRVGDELEVSAPRNLFPLDEAARRHLLIAGGIGITPILSMARALAARGA-DFELHYAGRSREDAAFLDELAALPG--DRV 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 266 EVHVVvarpdpdwDGRTGL-VTDLLDErmlASGDADVYLCGPVAMVDAART 315
Cdd:cd06185   154 HLHFD--------DEGGRLdLAALLAA---PPAGTHVYVCGPEGMMDAVRA 193
DHOD_e_trans cd06218
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. ...
 109-321 1.74e-13

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99814 [Multi-domain]  Cd Length: 246  Bit Score: 71.04  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGMAGALRyrAGQFAQLQVPGTN---VWRNYSYAHPADGRGECEFIIRLLPDG--VMSNYlr 183
Cdd:cd06218     1 VLSNREIADDIYRLVLEAPEIAAAAK--PGQFVMLRVPDGSdplLRRPISIHDVDPEEGTITLLYKVVGKGtrLLSEL-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 draQPGDHIAL-----RcskgSFYLRPIVRPVILVAGGTGLSAILAMAQSLdADVAHPVYLLYGVERTEDLCKLDELtel 258
Cdd:cd06218    77 ---KAGDELDVlgplgN----GFDLPDDDGKVLLVGGGIGIAPLLFLAKQL-AERGIKVTVLLGFRSADDLFLVEEF--- 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2522989786 259 rrrvGRLEVHVVVARPDPDWdGRTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWLDHNG 321
Cdd:cd06218   146 ----EALGAEVYVATDDGSA-GTKGFVTDLLKELLAEARPDVVYACGPEPMLKAVAELAAERG 203
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
12-84 3.65e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 65.24  E-value: 3.65e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786  12 DGTHKTMPVRCDQT-VLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEgLSDVERAARK-ILTCQTFVT 84
Cdd:pfam00111   4 NGKGVTIEVPDGETtLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDQSDQSF-LEDDELAAGYvVLACQTYPK 77
PLN02252 PLN02252
nitrate reductase [NADPH]
 144-313 4.05e-12

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 70.09  E-value: 4.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 144 QVPGTNVWRNYSYAHPADGRGECEFIIRL--------LPDG-VMSNYLrDRAQPGDHIALR--------CSKGSFYL--- 203
Cdd:PLN02252  676 TINGKLCMRAYTPTSSDDEVGHFELVIKVyfknvhpkFPNGgLMSQYL-DSLPIGDTIDVKgplghieyAGRGSFLVngk 754

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 204 RPIVRPVILVAGGTGLSAILAMAQSLDADVAHP--VYLLYGVERTEDLCKLDELTEL-RRRVGRLEVHVVVARPDP-DWD 279
Cdd:PLN02252  755 PKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKteMSLVYANRTEDDILLREELDRWaAEHPDRLKVWYVVSQVKReGWK 834

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2522989786 280 GRTGLVTDLLDERMLASGDADVY--LCGPVAMVDAA 313
Cdd:PLN02252  835 YSVGRVTEAMLREHLPEGGDETLalMCGPPPMIEFA 870
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 2-90 7.21e-12

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 62.47  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   2 AVRQVTVGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQT 81
Cdd:TIGR02008   1 ATYKVTLVNPDGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDQMEAGYVLTCVA 80


                  ....*....
gi 2522989786  82 FVTSDCRIE 90
Cdd:TIGR02008  81 YPTSDCTIE 89
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
19-312 1.21e-11

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 66.67  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  19 PVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSDCRIELQYPVDDN 98
Cdd:PRK05713   12 SVPAGSNLLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEKREQGWRLACQCRVVGDLRVEVFDPQRDG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  99 AALLVTGdgvvtaVELVSPSTAILRVDTsgmAGALRYRAGQFAQLQVPGtNVWRNYSYAHPADGRGECEFIIRLLPDGVM 178
Cdd:PRK05713   92 LPARVVA------LDWLGGDVLRLRLEP---ERPLRYRAGQHLVLWTAG-GVARPYSLASLPGEDPFLEFHIDCSRPGAF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 179 SNYLRdRAQPGDHIAL-RCSKGSFYLRP--IVRPVILVAGGTGLSAILA-MAQSLDADVAHPVYLLYgVERTEDLCKL-D 253
Cdd:PRK05713  162 CDAAR-QLQVGDLLRLgELRGGALHYDPdwQERPLWLLAAGTGLAPLWGiLREALRQGHQGPIRLLH-LARDSAGHYLaE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2522989786 254 ELTELRRRVGRLEVHVVVARPdpdwdgrtglVTDLLDERMLASGDADVYLCGPVAMVDA 312
Cdd:PRK05713  240 PLAALAGRHPQLSVELVTAAQ----------LPAALAELRLVSRQTMALLCGSPASVER 288
SiR_like2 cd06201
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 119-318 8.46e-11

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99798 [Multi-domain]  Cd Length: 289  Bit Score: 63.89  E-value: 8.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 119 TAILR---VDTSGMAGAL-RYRAGQFAQLQVPGTNVWRNYSYAHpADGRGECEFIIRLLPDGVMSNYLRDrAQPGDHIA- 193
Cdd:cd06201    64 TAILRfkpAKRKLSGKGLpSFEAGDLLGILPPGSDVPRFYSLAS-SSSDGFLEICVRKHPGGLCSGYLHG-LKPGDTIKa 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 194 -LRcSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDAdvAHPVYLLYGvERTEDLCKL--DELTELrRRVGRL-EVHV 269
Cdd:cd06201   142 fIR-PNPSFRPAKGAAPVILIGAGTGIAPLAGFIRANAA--RRPMHLYWG-GRDPASDFLyeDELDQY-LADGRLtQLHT 216

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2522989786 270 VVAR-PDPdwdgrtGLVTDLLDE------RMLASGdADVYLCGPVAMVDAARTWLD 318
Cdd:cd06201   217 AFSRtPDG------AYVQDRLRAdaerlrRLIEDG-AQIMVCGSRAMAQGVAAVLE 265
petF CHL00134
ferredoxin; Validated
 1-89 2.53e-10

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 57.81  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   1 MAVRQVT-VGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTC 79
Cdd:CHL00134    1 MATYKVTlLSEEEGIDVTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDQLEAGFVLTC 80

                          90
                  ....*....|
gi 2522989786  80 QTFVTSDCRI 89
Cdd:CHL00134   81 VAYPTSDCTI 90
CYPOR_like cd06182
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 116-307 6.01e-10

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. CYPOR has a C-terminal ferredoxin reducatase (FNR)- like FAD and NAD binding module, an FMN-binding domain, and an additional conecting domain (inserted within the FAD binding region) that orients the FNR and FMN binding domains. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2, which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99779 [Multi-domain]  Cd Length: 267  Bit Score: 60.81  E-value: 6.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 116 SPSTAILRVDTSGmAGALRYRAGQFA------QLQVpgtnvwRNYSYAH-PADGRGECEFIIRLL----PD-----GVMS 179
Cdd:cd06182    14 PRSTRHLEFDLSG-NSVLKYQPGDHLgvippnPLQP------RYYSIASsPDVDPGEVHLCVRVVsyeaPAgrirkGVCS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 180 NYLRDrAQPGDHIALRCSKG-SFYL-RPIVRPVILVAGGTGL----SAILAMAQSLDADVA-HPVYLLYGVER-TEDLCK 251
Cdd:cd06182    87 NFLAG-LQLGAKVTVFIRPApSFRLpKDPTTPIIMVGPGTGIapfrGFLQERAALRANGKArGPAWLFFGCRNfASDYLY 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2522989786 252 LDELTELRRRVGRLEVHVVVARpDPDWDGRtgLVTDLLDE------RMLaSGDADVYLCGPV 307
Cdd:cd06182   166 REELQEALKDGALTRLDVAFSR-EQAEPKV--YVQDKLKEhaeelrRLL-NEGAHIYVCGDA 223
PRK10926 PRK10926
ferredoxin-NADP reductase; Provisional
 137-310 1.28e-09

ferredoxin-NADP reductase; Provisional


Pssm-ID: 182844  Cd Length: 248  Bit Score: 59.71  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 137 AGQFAQL--QVPGTNVWRNYSYAH-PADGRgeCEFIIRLLPDGVMSNYLrDRAQPGDHIAL-RCSKGSFYLR--PIVRPV 210
Cdd:PRK10926   33 AGQFTKLglEIDGERVQRAYSYVNaPDNPD--LEFYLVTVPEGKLSPRL-AALKPGDEVQVvSEAAGFFVLDevPDCETL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQ-SLDADVAHPVYLLYGVERTEDLCKLDELTELRRRV-GRLEVHVVVARPDPDwDGRTGLVTDL 288
Cdd:PRK10926  110 WMLATGTAIGPYLSILQeGKDLERFKNLVLVHAARYAADLSYLPLMQELEQRYeGKLRIQTVVSRETAP-GSLTGRVPAL 188

                         170       180       190
                  ....*....|....*....|....*....|
gi 2522989786 289 LDERMLASG-----DAD---VYLCGPVAMV 310
Cdd:PRK10926  189 IESGELEAAvglpmDAEtshVMLCGNPQMV 218
SiR_like1 cd06200
Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta ...
 116-305 2.02e-09

Cytochrome p450- like alpha subunits of E. coli sulfite reductase (SiR) multimerize with beta subunits to catalyze the NADPH dependent reduction of sulfite to sulfide. Beta subunits have an Fe4S4 cluster and a siroheme, while the alpha subunits (cysJ gene) are of the cytochrome p450 (CyPor) family having FAD and FMN as prosthetic groups and utilizing NADPH. Cypor (including cyt -450 reductase, nitric oxide synthase, and methionine synthase reductase) are ferredoxin reductase (FNR)-like proteins with an additional N-terminal FMN domain and a connecting sub-domain inserted within the flavin binding portion of the FNR-like domain. The connecting domain orients the N-terminal FMN domain with the C-terminal FNR domain. NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues, and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule, which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99797  Cd Length: 245  Bit Score: 58.83  E-value: 2.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 116 SPSTAILRVDTSGMAGALRYRAGQFAQLQVPGTNVWRNYSYAH-PADGrgECEFIIRLLPD-----GVMSNYLRDRAQPG 189
Cdd:cd06200    13 SQGAPLWRLRLTPPDAGAQWQAGDIAEIGPRHPLPHREYSIASlPADG--ALELLVRQVRHadgglGLGSGWLTRHAPIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 190 DHIALRC-SKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADVAHPVYLLYGvERTED---LCKlDELTELRRRvGRL 265
Cdd:cd06200    91 ASVALRLrENPGFHLPDDGRPLILIGNGTGLAGLRSHLRARARAGRHRNWLLFG-ERQAAhdfFCR-EELEAWQAA-GHL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2522989786 266 E-VHVVVARPDPDwdgrTGLVTDLLDERM------LASGdADVYLCG 305
Cdd:cd06200   168 ArLDLAFSRDQAQ----KRYVQDRLRAAAdelrawVAEG-AAIYVCG 209
PRK08345 PRK08345
cytochrome-c3 hydrogenase subunit gamma; Provisional
 135-309 4.99e-09

cytochrome-c3 hydrogenase subunit gamma; Provisional


Pssm-ID: 236247 [Multi-domain]  Cd Length: 289  Bit Score: 58.28  E-value: 4.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 135 YRAGQFAQLQVPGTNVWrNYSYAHPADGRGECEFIIRLLpdGVMSNYLRdRAQPGDHIALRCSKGSFYlrPIVR----PV 210
Cdd:PRK08345   38 FKPGQFVQVTIPGVGEV-PISICSSPTRKGFFELCIRRA--GRVTTVIH-RLKEGDIVGVRGPYGNGF--PVDEmegmDL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 211 ILVAGGTGLSAILAMAQ-SLDADVAH-PVYLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARpDPDWDGRTGL---- 284
Cdd:PRK08345  112 LLIAGGLGMAPLRSVLLyAMDNRWKYgNITLIYGAKYYEDLLFYDELIKDLAEAENVKIIQSVTR-DPEWPGCHGLpqgf 190

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2522989786 285 --------VTDLLDERMLASGDADVYLCGPVAM 309
Cdd:PRK08345  191 iervckgvVTDLFREANTDPKNTYAAICGPPVM 223
bifunctional_CYPOR cd06206
These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase ...
 175-314 2.76e-08

These bifunctional proteins fuse N-terminal cytochrome p450 with a cytochrome p450 reductase (CYPOR). NADPH cytochrome p450 reductase serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99802 [Multi-domain]  Cd Length: 384  Bit Score: 56.88  E-value: 2.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 175 DGVMSNYLrDRAQPGDHI--ALRCSKGSFYLRPIVR-PVILVAGGTGLSAILAMAQSLDADVAH-----PVYLLYGVeRT 246
Cdd:cd06206   196 RGVASSYL-SSLRPGDSIhvSVRPSHSAFRPPSDPStPLIMIAAGTGLAPFRGFLQERAALLAQgrklaPALLFFGC-RH 273

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2522989786 247 EDLCKL--DELTELRRRvGRLEVHVVVARPDpdwDGRTGLVTDLL-DER-----MLASGdADVYLCGPVAMVDAAR 314
Cdd:cd06206   274 PDHDDLyrDELEEWEAA-GVVSVRRAYSRPP---GGGCRYVQDRLwAEReevweLWEQG-ARVYVCGDGRMAPGVR 344
PRK00054 PRK00054
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
 109-309 3.13e-08

dihydroorotate dehydrogenase electron transfer subunit; Reviewed


Pssm-ID: 234601 [Multi-domain]  Cd Length: 250  Bit Score: 55.26  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGmagALRYRAGQFAQLQVPGTNV--WRNYSYAHPadGRGECEFIIRLLPDG--VMSNYlrd 184
Cdd:PRK00054    9 IVENKEIAPNIYTLVLDGEK---VFDMKPGQFVMVWVPGVEPllERPISISDI--DKNEITILYRKVGEGtkKLSKL--- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 185 raQPGDHIALRCSKGS-FYLRPIVRPVILVAGGTGLSAILAMAQSLDADVAHPVYLLYGVERTEDLCkLDELtelrRRVG 263
Cdd:PRK00054   81 --KEGDELDIRGPLGNgFDLEEIGGKVLLVGGGIGVAPLYELAKELKKKGVEVTTVLGARTKDEVIF-EEEF----AKVG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2522989786 264 rlEVHVVVarpDPDWDGRTGLVTDLLDERMLaSGDAdVYLCGPVAM 309
Cdd:PRK00054  154 --DVYVTT---DDGSYGFKGFVTDVLDELDS-EYDA-IYSCGPEIM 192
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 112-332 4.27e-08

NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.


Pssm-ID: 99783 [Multi-domain]  Cd Length: 210  Bit Score: 54.23  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 112 VELVSPSTAI-LRVDTSGMagaLRYRAGQFAQLQVPgtNVWRNYSYaHP-------ADGRGECEFIIRLLpDGVMSNYLR 183
Cdd:cd06186     4 VELLPDSDVIrLTIPKPKP---FKWKPGQHVYLNFP--SLLSFWQS-HPftiasspEDEQDTLSLIIRAK-KGFTTRLLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 184 DraqpgdhiALRCSKGSFYLR--------PIVRP------VILVAGGTGLSAILAMAQSL-----DADVAHPVYLLYGVE 244
Cdd:cd06186    77 K--------ALKSPGGGVSLKvlvegpygSSSEDllsydnVLLVAGGSGITFVLPILRDLlrrssKTSRTRRVKLVWVVR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 245 RTEDLCKL-DELTELRRRVGRLEVHVVVARpdpdwdgrtglvtdlldermlasgdadVYLCGPVAMVDAARTWLDHNGFH 323
Cdd:cd06186   149 DREDLEWFlDELRAAQELEVDGEIEIYVTR---------------------------VVVCGPPGLVDDVRNAVAKKGGT 201


                  ....*....
gi 2522989786 324 RVGLYYEKF 332
Cdd:cd06186   202 GVEFHEESF 210
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 134-332 8.34e-08

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 55.10  E-value: 8.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 134 RYRAGQFAQLQVPGT-NVWRNYSYAHPAdgrGECEFI---IRLLPDGVMSNYLRDRAQPGDHIALRCSKGSFYLRPIVRP 209
Cdd:PRK10684   36 PYRAGQYALVSIRNSaETLRAYTLSSTP---GVSEFItltVRRIDDGVGSQWLTRDVKRGDYLWLSDAMGEFTCDDKAED 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 210 -VILVAGGTGLSAILAMAQSL-----DADVAhpvyLLYGVERTEDLCKLDELTELRRRVGRLEVHVVVARPDPDwdgrtG 283
Cdd:PRK10684  113 kYLLLAAGCGVTPIMSMRRWLlknrpQADVQ----VIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVAENNATE-----G 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2522989786 284 LVTDLLDERMLASGDAD-----VYLCGPVAMVDAARTWLDHNGFHRVGLYYEKF 332
Cdd:PRK10684  184 FIAGRLTRELLQQAVPDlasrtVMTCGPAPYMDWVEQEVKALGVTADRFFKEKF 237
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 116-309 1.08e-07

FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 53.41  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 116 SPSTAILRVDtsgmaGALRYRAGQFAQLQVPGTN-VWRNYSYAHPADGrgecefiIRLLPDGVMSNYLRDRAqPGDHIAL 194
Cdd:cd06220    10 TPTVKTFVFD-----WDFDFKPGQFVMVWVPGVDeIPMSLSYIDGPNS-------ITVKKVGEATSALHDLK-EGDKLGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 195 RCSKGSFYlRPIVRPVILVAGGTGLSAILAMAQSLDADVAhpVYLLYGVERTEDLCKLDELtelrRRVGRlevhVVVARP 274
Cdd:cd06220    77 RGPYGNGF-ELVGGKVLLIGGGIGIAPLAPLAERLKKAAD--VTVLLGARTKEELLFLDRL----RKSDE----LIVTTD 145

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2522989786 275 DPDWdGRTGLVTDLLDERMLASGDAdVYLCGPVAM 309
Cdd:cd06220   146 DGSY-GFKGFVTDLLKELDLEEYDA-IYVCGPEIM 178
ViuB COG2375
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ...
 109-317 1.38e-07

NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];


Pssm-ID: 441942 [Multi-domain]  Cd Length: 260  Bit Score: 53.73  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGMAGALRYRAGQFAQLQVP---------------------GTNVWRNYSYAHPADGRGECE 167
Cdd:COG2375    20 VVRVERLSPHMRRVTLGGEDLAGFASPGPDDHVKLFFPppgggepvlptlddglalpgeERPVMRTYTVRRFDPEAGELD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 168 FIIRL-LPDGVMSNYLRdRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADVahPVYLLYGVERT 246
Cdd:COG2375   100 IDFVLhGDGGPASRWAA-RARPGDRVGILGPGGSFVPPPDADWYLLAGDETALPAIARILEALPADA--RGTAVIEVPDA 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 247 EDLCKLDELtelrrrvGRLEVHVVVARPDPDwdgrTGLVTDLLDERMLASGDADVYLCGPVAMVDAARTWL 317
Cdd:COG2375   177 ADEQPLPAP-------AGVEVTWLHRGGAPP----GSALLDAVRALELPDGDVYAWVAGEASAVRALRRHL 236
PA_CoA_Oxy5 TIGR02160
phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised ...
 3-86 5.28e-07

phenylacetate-CoA oxygenase/reductase, PaaK subunit; Phenylacetate-CoA oxygenase is comprised of a five gene complex responsible for the hydroxylation of phenylacetate-CoA (PA-CoA) as the second catabolic step in phenylacetic acid (PA) degradation. Although the exact function of this enzyme has not been determined, it has been shown to be required for phenylacetic acid degradation and has been proposed to function in a multicomponent oxygenase acting on phenylacetate-CoA. [Energy metabolism, Other]


Pssm-ID: 131215 [Multi-domain]  Cd Length: 352  Bit Score: 52.52  E-value: 5.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786   3 VRQVTVGYSDGTHKTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTF 82
Cdd:TIGR02160 262 VSKVTVTLDGRSTETSSLSRDESVLDAALRARPDLPFACKGGVCGTCRAKVLEGKVDMERNYALEPDEVDAGYVLTCQAY 341


                  ....
gi 2522989786  83 VTSD 86
Cdd:TIGR02160 342 PLSD 345
PLN03136 PLN03136
Ferredoxin; Provisional
 20-90 5.67e-07

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 49.75  E-value: 5.67e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2522989786  20 VRCDQTV--LDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSDCRIE 90
Cdd:PLN03136   68 VECEEDVyvLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDEQISEGYVLTCVAYPTSDVVIE 140
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 150-313 1.77e-06

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 50.60  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 150 VWRNYSYAHPADGRGECEFIIRL--------LPDG-VMSNYLrDRAQPGDHIALRCSKGSF-YLRP------------IV 207
Cdd:PTZ00319   85 VQHSYTPISSDDEKGYVDFLIKVyfkgvhpsFPNGgRLSQHL-YHMKLGDKIEMRGPVGKFeYLGNgtytvhkgkgglKT 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 208 RPV---ILVAGGTGLSAILAMAQSLDADVAHP--VYLLYGVERTEDLCKLDELTELRRRvGRLEV-HVVVARPDPDWDGR 281
Cdd:PTZ00319  164 MHVdafAMIAGGTGITPMLQIIHAIKKNKEDRtkVFLVYANQTEDDILLRKELDEAAKD-PRFHVwYTLDREATPEWKYG 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2522989786 282 TGLVTD--------LLDERMLASGDADVYLCGPVAMVDAA 313
Cdd:PTZ00319  243 TGYVDEemlrahlpVPDPQNSGIKKVMALMCGPPPMLQMA 282
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 109-319 9.30e-06

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 47.71  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDtSGMAGALrYRAGQFAQLQVPGTN--VWRNYS--YAHPADGRgeCEFIIrlLPDGVMSNYLRD 184
Cdd:cd06192     1 IVKKEQLEPNLVLLTIK-APLAARL-FRPGQFVFLRNFESPglERIPLSlaGVDPEEGT--ISLLV--EIRGPKTKLIAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 185 RaQPGDHIALRcskgSFYLRPIVRP-----VILVAGGTGLSAILAMAQSLDADvAHPVYLLYGVERTEDLCKLDELtelr 259
Cdd:cd06192    75 L-KPGEKLDVM----GPLGNGFEGPkkggtVLLVAGGIGLAPLLPIAKKLAAN-GNKVTVLAGAKKAKEEFLDEYF---- 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2522989786 260 rrvgRLEVHVVVARPDPDWDGRTGLVTDLLDERMLASGDAdVYLCGPVAM----VDAARTWLDH 319
Cdd:cd06192   145 ----ELPADVEIWTTDDGELGLEGKVTDSDKPIPLEDVDR-IIVAGSDIMmkavVEALDEWLQL 203
CyPoR_like cd06207
NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase ...
 176-306 2.32e-05

NADPH cytochrome p450 reductase (CYPOR) serves as an electron donor in several oxygenase systems and is a component of nitric oxide synthases and methionine synthase reductases. CYPOR transfers two electrons from NADPH to the heme of cytochrome p450 via FAD and FMN. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99803 [Multi-domain]  Cd Length: 382  Bit Score: 47.65  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 176 GVMSNYLRdRAQPGDHIALRCSKGSFYL-RPIVRPVILVAGGTGLSAILAMAQSLDADVAH-----PVYLLYGV--ERTE 247
Cdd:cd06207   199 GLCSSYLA-GLKVGQRVTVFIKKSSFKLpKDPKKPIIMVGPGTGLAPFRAFLQERAALLAQgpeigPVLLYFGCrhEDKD 277

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2522989786 248 DLCKlDELTELRRRVGRLEVHVVVARPDPdwdgRTGLVTDLLDE------RMLASGDADVYLCGP 306
Cdd:cd06207   278 YLYK-EELEEYEKSGVLTTLGTAFSRDQP----KKVYVQDLIREnsdlvyQLLEEGAGVIYVCGS 337
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 167-321 2.76e-05

Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which varies in orientation with respect to the NAD(P) binding domain. The N-terminal region may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 46.08  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 167 EFIIRLLPD--GVmSNYLRdRAQPGDHIALRCSKGSFYLRPivrPVILVAGGTGLSAILAMAQSLDADVAHPVYLLYGVE 244
Cdd:cd06196    62 EFVIKSYPDhdGV-TEQLG-RLQPGDTLLIEDPWGAIEYKG---PGVFIAGGAGITPFIAILRDLAAKGKLEGNTLIFAN 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 245 RTED--LCKldelTELRRRVGRLEVHVVVARPDPDWDGRtglvtdLLDERMLAS----GDADVYLCGPVAMVDAARTWLD 318
Cdd:cd06196   137 KTEKdiILK----DELEKMLGLKFINVVTDEKDPGYAHG------RIDKAFLKQhvtdFNQHFYVCGPPPMEEAINGALK 206


                  ...
gi 2522989786 319 HNG 321
Cdd:cd06196   207 ELG 209
PTZ00038 PTZ00038
ferredoxin; Provisional
 23-90 3.08e-05

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 45.60  E-value: 3.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2522989786  23 DQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSDCRIE 90
Cdd:PTZ00038  114 DEYILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEQLKKGYCLLCTCYPKSDCTIE 181
siderophore_interacting cd06193
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ...
 109-317 1.09e-04

Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99790 [Multi-domain]  Cd Length: 235  Bit Score: 44.56  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 109 VTAVELVSPSTAILRVDTSGMAGALRYRAGQ------------FAQLQVPGTNVW---------RNYSYAHPADGRGECE 167
Cdd:cd06193     1 VVRVERLTPHMRRITLGGPDLAGFPSDGPDQhvkllfpdpgqaPPVLPVLGRRRWppeeprpvmRTYTVRRFDPEAGELD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 168 FIIRLLPD-GVMSNYLRdRAQPGDHIALRCSKGSFYLRPIVRPVILVAGGTGLSAILAMAQSLDADVahPVYLLYGVERT 246
Cdd:cd06193    81 IDFVLHGDeGPASRWAA-SAQPGDTLGIAGPGGSFLPPPDADWYLLAGDETALPAIAAILEELPADA--RGTALIEVPDA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786 247 EDLCKLDeltelrrRVGRLEVHVVVARPDPDWDGRTGLVTDLLdermLASGDADVYLCGPVAMVDAARTWL 317
Cdd:cd06193   158 ADEQPLP-------APAGVEVTWLHRGGAEAGELALLAVRALA----PPAGDGYVWIAGEAGAVRALRRHL 217
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 16-86 2.56e-04

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 43.93  E-value: 2.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2522989786  16 KTMPVRCDQTVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMGRTEGLSDVERAARKILTCQTFVTSD 86
Cdd:PRK10684  258 REFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPAEIAQGYVLACSCHPQGD 328
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 187-309 3.65e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 44.39  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786  187 QPGDH----------IALRCSKGSFYLRP-IVRPVILVAGGTGLSailAMAQSLDADVAHP-------VYLLYGVERTED 248
Cdd:PTZ00306  1000 RPGDSvemkacgglrIERRPADKQFVFRGhVIRKLALIAGGTGVA---PMLQIIRAALKKPyvdsiesIRLIYAAEDVSE 1076

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2522989786  249 LCKLDELTELRRR-VGRLEVHVVVARPDPDWDGRTGLVTDLLDERML--ASGDADVYLCGPVAM 309
Cdd:PTZ00306  1077 LTYRELLESYRKEnPGKFKCHFVLNNPPEGWTDGVGFVDRALLQSALqpPSKDLLVAICGPPVM 1140
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 364-551 1.16e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 41.85  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 364 AVVIGGSIAGIAAAKMLSETFDRVIVLEKDgPHRRREGRPGAaqgwhLHHlltAGQIELERIfpGIVDDMVREGAfkVDM 443
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERA-PPPRPDGRGIA-----LSP---RSLELLRRL--GLWDRLLARGA--PIR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2522989786 444 AAQYRIRLGGTWKK----PGTSDIEIVCAGRPLLEWCVRRRLDDEPrIDFRYESEVADLAFDRAnnaivGVAVDNGDAdg 519
Cdd:COG0654    73 GIRVRDGSDGRVLArfdaAETGLPAGLVVPRADLERALLEAARALG-VELRFGTEVTGLEQDAD-----GVTVTLADG-- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2522989786 520 gdglQVVPAEFVVDASGKNTRVPEFLERLGVG 551
Cdd:COG0654   145 ----RTLRADLVVGADGARSAVRRLLGIGFTG 172
PLN02268 PLN02268
probable polyamine oxidase
 363-391 2.17e-03

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 41.21  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 2522989786 363 TAVVIGGSIAGIAAAKMLSETFDRVIVLE 391
Cdd:PLN02268    2 SVIVIGGGIAGIAAARALHDASFKVTLLE 30
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
25-91 2.49e-03

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 37.79  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2522989786  25 TVLDAAEEHGVAIVNECQSGICGTCVATCTAGRYQMgRTEGLSDVERAarKILTCQTFVTSDCRIEL 91
Cdd:PRK10713   21 SLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDW-IAEPLAFIQPG--EILPCCCRAKGDIEIEM 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH